메뉴 건너뛰기




Volumn 2, Issue 6, 2013, Pages

Autoantibodies targeting tumor-associated antigens in metastatic cancer Sialylated iggs as candidate anti-inflammatory antibodies

Author keywords

Anti inflammatory; DC SIGN; Glycosylation; HER 2 neu; IgG; NY ESO 1; Sialic acid; Tumor immunity

Indexed keywords

AGGLUTININ; ALPHA 2,6 SIALIC ACID; ANTIBODY; ANTIINFLAMMATORY ANTIBODY; AUTOANTIBODY; CD209 ANTIGEN; EPIDERMAL GROWTH FACTOR RECEPTOR 2; FC RECEPTOR; GLYCAN DERIVATIVE; IMMUNOGLOBULIN F(AB) FRAGMENT; IMMUNOGLOBULIN G ANTIBODY; IMMUNOGLOBULIN HEAVY CHAIN; IMMUNOGLOBULIN LIGHT CHAIN; INTERCELLULAR ADHESION MOLECULE 2; INTERCELLULAR ADHESION MOLECULE 3; NY ESO 1 ANTIGEN; SAMBUCUS NIGRA AGGLUTININ; SIALIC ACID; SIALYLTRANSFERASE; TUMOR ANTIGEN; UNCLASSIFIED DRUG;

EID: 84886945075     PISSN: 21624011     EISSN: 2162402X     Source Type: Journal    
DOI: 10.4161/onci.24841     Document Type: Article
Times cited : (16)

References (63)
  • 1
    • 13344282077 scopus 로고
    • Human neoplasms elicit multiple specific immune responses in the autologous host
    • USA, PMID:8524854
    • Sahin U, Türeci O, Schmitt H, Cochlovius B, Johannes T, Schmits R, et al. Human neoplasms elicit multiple specific immune responses in the autologous host. Proc Natl Acad Sci U S A 1995; 92:11810-3; PMID:8524854; http://dx.doi.org/10.1073/pnas.92.25.11810
    • (1995) Proc Natl Acad Sci , vol.92 , pp. 11810-3
    • Sahin, U.1    Türeci, O.2    Schmitt, H.3    Cochlovius, B.4    Johannes, T.5    Schmits, R.6
  • 2
    • 68549106119 scopus 로고    scopus 로고
    • A systematic review of humoral immune responses against tumor antigens
    • PMID:19562338
    • Reuschenbach M, von Knebel Doeberitz M, Wentzensen N. A systematic review of humoral immune responses against tumor antigens. Cancer Immunol Immunother 2009; 58:1535-44; PMID:19562338; http://dx.doi. org/10.1007/s00262-009-0733-4
    • (2009) Cancer Immunol Immunother , vol.58 , pp. 1535-1544
    • Reuschenbach, M.1    von Knebel Doeberitz, M.2    Wentzensen, N.3
  • 3
    • 77953914685 scopus 로고    scopus 로고
    • Autoantibodies against tumor-related antigens: incidence and biologic significance
    • PMID:20433885
    • Kobold S, Lütkens T, Cao Y, Bokemeyer C, Atanackovic D. Autoantibodies against tumor-related antigens: incidence and biologic significance. Hum Immunol 2010; 71:643-51; PMID:20433885; http://dx.doi.org/10.1016/j.humimm.2010.03.015
    • (2010) Hum Immunol , vol.71 , pp. 643-651
    • Kobold, S.1    Lütkens, T.2    Cao, Y.3    Bokemeyer, C.4    Atanackovic, D.5
  • 4
    • 79953151458 scopus 로고    scopus 로고
    • Cancer immunoediting: integrating immunity's roles in cancer suppression and promotion
    • PMID:21436444
    • Schreiber RD, Old LJ, Smyth MJ. Cancer immunoediting: integrating immunity's roles in cancer suppression and promotion. Science 2011; 331:1565-70; PMID:21436444; http://dx.doi.org/10.1126/science. 1203486
    • (2011) Science , vol.331 , pp. 1565-1570
    • Schreiber, R.D.1    Old, L.J.2    Smyth, M.J.3
  • 5
    • 0034162485 scopus 로고    scopus 로고
    • Mice bearing late-stage tumors have normal functional systemic T cell responses in vitro and in vivo
    • PMID:10679101
    • Radoja S, Rao TD, Hillman D, Frey AB. Mice bearing late-stage tumors have normal functional systemic T cell responses in vitro and in vivo. J Immunol 2000; 164:2619-28; PMID:10679101
    • (2000) J Immunol , vol.164 , pp. 2619-2628
    • Radoja, S.1    Rao, T.D.2    Hillman, D.3    Frey, A.B.4
  • 6
    • 79953059789 scopus 로고    scopus 로고
    • Natural innate and adaptive immunity to cancer
    • PMID:21219185
    • Vesely MD, Kershaw MH, Schreiber RD, Smyth MJ. Natural innate and adaptive immunity to cancer. Annu Rev Immunol 2011; 29:235-71; PMID:21219185; http://dx.doi.org/10.1146/annurevimmunol- 031210-101324
    • (2011) Annu Rev Immunol , vol.29 , pp. 235-271
    • Vesely, M.D.1    Kershaw, M.H.2    Schreiber, R.D.3    Smyth, M.J.4
  • 7
    • 84934440448 scopus 로고    scopus 로고
    • Inhibitory B7 family members in human ovarian carcinoma
    • PMID:18546634
    • Wei S, Curiel T, Coukos G, Liu R, Zou W. Inhibitory B7 family members in human ovarian carcinoma. Adv Exp Med Biol 2008; 622:261-71; PMID:18546634; http://dx.doi.org/10.1007/978-0-387-68969-2_21
    • (2008) Adv Exp Med Biol , vol.622 , pp. 261-271
    • Wei, S.1    Curiel, T.2    Coukos, G.3    Liu, R.4    Zou, W.5
  • 8
    • 44349150012 scopus 로고    scopus 로고
    • Inhibitory B7-family molecules in the tumour microenvironment
    • PMID:18500231
    • Zou W, Chen L. Inhibitory B7-family molecules in the tumour microenvironment. Nat Rev Immunol 2008; 8:467-77; PMID:18500231; http://dx.doi. org/10.1038/nri2326
    • (2008) Nat Rev Immunol , vol.8 , pp. 467-477
    • Zou, W.1    Chen, L.2
  • 9
    • 77950283280 scopus 로고    scopus 로고
    • Tumor cell expression of programmed cell death-1 ligand 1 is a prognostic factor for malignant melanoma
    • PMID:20143437
    • Hino R, Kabashima K, Kato Y, Yagi H, Nakamura M, Honjo T, et al. Tumor cell expression of programmed cell death-1 ligand 1 is a prognostic factor for malignant melanoma. Cancer 2010; 116:1757-66; PMID:20143437; http://dx.doi.org/10.1002/cncr.24899
    • (2010) Cancer , vol.116 , pp. 1757-1766
    • Hino, R.1    Kabashima, K.2    Kato, Y.3    Yagi, H.4    Nakamura, M.5    Honjo, T.6
  • 10
    • 34247122497 scopus 로고    scopus 로고
    • The impact of glycosylation on the biological function and structure of human immunoglobulins
    • PMID:17029568
    • Arnold JN, Wormald MR, Sim RB, Rudd PM, Dwek RA. The impact of glycosylation on the biological function and structure of human immunoglobulins. Annu Rev Immunol 2007; 25:21-50; PMID:17029568; http://dx.doi.org/10.1146/annurev. immunol.25.022106.141702
    • (2007) Annu Rev Immunol , vol.25 , pp. 21-50
    • Arnold, J.N.1    Wormald, M.R.2    Sim, R.B.3    Rudd, P.M.4    Dwek, R.A.5
  • 11
    • 28844463354 scopus 로고    scopus 로고
    • Control of recombinant monoclonal antibody effector functions by Fc N-glycan remodeling in vitro
    • PMID:16321047
    • Hodoniczky J, Zheng YZ, James DC. Control of recombinant monoclonal antibody effector functions by Fc N-glycan remodeling in vitro. Biotechnol Prog 2005; 21:1644-52; PMID:16321047; http://dx.doi. org/10.1021/bp050228w
    • (2005) Biotechnol Prog , vol.21 , pp. 1644-1652
    • Hodoniczky, J.1    Zheng, Y.Z.2    James, D.C.3
  • 12
    • 0037178791 scopus 로고    scopus 로고
    • Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity
    • PMID:11986321
    • Shields RL, Lai J, Keck R, O'Connell LY, Hong K, Meng YG, et al. Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity. J Biol Chem 2002; 277:26733-40; PMID:11986321; http://dx.doi.org/10.1074/jbc. M202069200
    • (2002) J Biol Chem , vol.277 , pp. 26733-40
    • Shields, R.L.1    Lai, J.2    Keck, R.3    O'Connell, L.Y.4    Hong, K.5    Meng, Y.G.6
  • 13
    • 33750835115 scopus 로고    scopus 로고
    • Non-fucosylated therapeutic antibodies as next-generation therapeutic antibodies
    • PMID:17049014
    • Satoh M, Iida S, Shitara K. Non-fucosylated therapeutic antibodies as next-generation therapeutic antibodies. Expert Opin Biol Ther 2006; 6:1161-73; PMID:17049014; http://dx.doi. org/10.1517/14712598.6.11.1161
    • (2006) Expert Opin Biol Ther , vol.6 , pp. 1161-1173
    • Satoh, M.1    Iida, S.2    Shitara, K.3
  • 14
    • 33746888249 scopus 로고    scopus 로고
    • Antiinflammatory activity of immunoglobulin G resulting from Fc sialylation
    • PMID:16888140
    • Kaneko Y, Nimmerjahn F, Ravetch JV. Antiinflammatory activity of immunoglobulin G resulting from Fc sialylation. Science 2006; 313:670-3; PMID:16888140; http://dx.doi.org/10.1126/science. 1129594
    • (2006) Science , vol.313 , pp. 670-673
    • Kaneko, Y.1    Nimmerjahn, F.2    Ravetch, J.V.3
  • 15
    • 33751253486 scopus 로고    scopus 로고
    • Higher levels of sialylated Fc glycans in immunoglobulin G molecules can adversely impact functionality
    • PMID:17045339
    • Scallon BJ, Tam SH, McCarthy SG, Cai AN, Raju TS. Higher levels of sialylated Fc glycans in immunoglobulin G molecules can adversely impact functionality. Mol Immunol 2007; 44:1524-34; PMID:17045339; http://dx.doi.org/10.1016/j.molimm.2006.09.005
    • (2007) Mol Immunol , vol.44 , pp. 1524-1534
    • Scallon, B.J.1    Tam, S.H.2    McCarthy, S.G.3    Cai, A.N.4    Raju, T.S.5
  • 16
    • 79960046406 scopus 로고    scopus 로고
    • Intravenous gammaglobulin suppresses inflammation through a novel T(H)2 pathway
    • PMID:21685887
    • Anthony RM, Kobayashi T, Wermeling F, Ravetch JV. Intravenous gammaglobulin suppresses inflammation through a novel T(H)2 pathway. Nature 2011; 475:110-3; PMID:21685887; http://dx.doi. org/10.1038/nature10134
    • (2011) Nature , vol.475 , pp. 110-113
    • Anthony, R.M.1    Kobayashi, T.2    Wermeling, F.3    Ravetch, J.V.4
  • 17
    • 58149378347 scopus 로고    scopus 로고
    • Identification of a receptor required for the antiinflammatory activity of IVIG
    • PMID:19036920
    • Anthony RM, Wermeling F, Karlsson MC, Ravetch JV. Identification of a receptor required for the antiinflammatory activity of IVIG. Proc Natl Acad Sci U S A 2008; 105:19571-8; PMID:19036920; http://dx.doi.org/10.1073/pnas.0810163105
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 19571-8
    • Anthony, R.M.1    Wermeling, F.2    Karlsson, M.C.3    Ravetch, J.V.4
  • 18
    • 33846423857 scopus 로고    scopus 로고
    • The antiinflammatory activity of IgG: the intravenous IgG paradox
    • PMID:17227911
    • Nimmerjahn F, Ravetch JV. The antiinflammatory activity of IgG: the intravenous IgG paradox. J Exp Med 2007; 204:11-5; PMID:17227911; http://dx.doi. org/10.1084/jem.20061788
    • (2007) J Exp Med , vol.204 , pp. 11-15
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 19
    • 77956185954 scopus 로고    scopus 로고
    • A novel role for the IgG Fc glycan: the anti-inflammatory activity of sialylated IgG Fcs
    • PMID:20480216
    • Anthony RM, Ravetch JV. A novel role for the IgG Fc glycan: the anti-inflammatory activity of sialylated IgG Fcs. J Clin Immunol 2010; 30(Suppl 1):S9-14; PMID:20480216; http://dx.doi.org/10.1007/s10875-010-9405-6
    • (2010) J Clin Immunol , vol.30 , Issue.SUPPL 1
    • Anthony, R.M.1    Ravetch, J.V.2
  • 20
    • 84860235393 scopus 로고    scopus 로고
    • Novel roles for the IgG Fc glycan
    • PMID:22288459
    • Anthony RM, Wermeling F, Ravetch JV. Novel roles for the IgG Fc glycan. Ann N Y Acad Sci 2012; 1253:170-80; PMID:22288459; http://dx.doi.org/10.1111/j.1749-6632.2011.06305.x
    • (2012) Ann N Y Acad Sci , vol.1253 , pp. 170-180
    • Anthony, R.M.1    Wermeling, F.2    Ravetch, J.V.3
  • 21
    • 31744447070 scopus 로고    scopus 로고
    • Glycosylation in the Fc domain of IgG increases resistance to proteolytic cleavage by papain
    • PMID:16442075
    • Raju TS, Scallon BJ. Glycosylation in the Fc domain of IgG increases resistance to proteolytic cleavage by papain. Biochem Biophys Res Commun 2006; 341:797-803; PMID:16442075; http://dx.doi.org/10.1016/j. bbrc.2006.01.030
    • (2006) Biochem Biophys Res Commun , vol.341 , pp. 797-803
    • Raju, T.S.1    Scallon, B.J.2
  • 22
    • 48949089988 scopus 로고    scopus 로고
    • Analysis of immunoglobulin glycosylation by LC-ESI-MS of glycopeptides and oligosaccharides
    • PMID:18655055
    • Stadlmann J, Pabst M, Kolarich D, Kunert R, Altmann F. Analysis of immunoglobulin glycosylation by LC-ESI-MS of glycopeptides and oligosaccharides. Proteomics 2008; 8:2858-71; PMID:18655055; http://dx.doi.org/10.1002/pmic.200700968
    • (2008) Proteomics , vol.8 , pp. 2858-2871
    • Stadlmann, J.1    Pabst, M.2    Kolarich, D.3    Kunert, R.4    Altmann, F.5
  • 23
    • 69949107840 scopus 로고    scopus 로고
    • A close look at human IgG sialylation and subclass distribution after lectin fractionation
    • PMID:19688751
    • Stadlmann J, Weber A, Pabst M, Anderle H, Kunert R, Ehrlich HJ, et al. A close look at human IgG sialylation and subclass distribution after lectin fractionation. Proteomics 2009; 9:4143-53; PMID:19688751; http://dx.doi.org/10.1002/pmic.200800931
    • (2009) Proteomics , vol.9 , pp. 4143-4153
    • Stadlmann, J.1    Weber, A.2    Pabst, M.3    Anderle, H.4    Kunert, R.5    Ehrlich, H.J.6
  • 24
    • 0030657467 scopus 로고    scopus 로고
    • High-titer HER-2/neu protein-specific antibody can be detected in patients with earlystage breast cancer
    • PMID:9363867
    • Disis ML, Pupa SM, Gralow JR, Dittadi R, Menard S, Cheever MA. High-titer HER-2/neu protein-specific antibody can be detected in patients with earlystage breast cancer. J Clin Oncol 1997; 15:3363-7; PMID:9363867
    • (1997) J Clin Oncol , vol.15 , pp. 3363-3367
    • Disis, M.L.1    Pupa, S.M.2    Gralow, J.R.3    Dittadi, R.4    Menard, S.5    Cheever, M.A.6
  • 25
    • 41649114135 scopus 로고    scopus 로고
    • Level of HER-2/neu protein expression in breast cancer may affect the development of endogenous HER-2/neu-specific immunity
    • PMID:18319334
    • Goodell V, Waisman J, Salazar LG, de la Rosa C, Link J, Coveler AL, et al. Level of HER-2/neu protein expression in breast cancer may affect the development of endogenous HER-2/neu-specific immunity. Mol Cancer Ther 2008; 7:449-54; PMID:18319334; http://dx.doi.org/10.1158/1535-7163.MCT-07-0386
    • (2008) Mol Cancer Ther , vol.7 , pp. 449-454
    • Goodell, V.1    Waisman, J.2    Salazar, L.G.3    de la Rosa, C.4    Link, J.5    Coveler, A.L.6
  • 26
    • 40649124272 scopus 로고    scopus 로고
    • Autoantibodies in lung cancer: possibilities for early detection and subsequent cure
    • PMID:17932110
    • Chapman CJ, Murray A, McElveen JE, Sahin U, Luxemburger U, Türeci O, et al. Autoantibodies in lung cancer: possibilities for early detection and subsequent cure. Thorax 2008; 63:228-33; PMID:17932110; http://dx.doi.org/10.1136/thx.2007.083592
    • (2008) Thorax , vol.63 , pp. 228-233
    • Chapman, C.J.1    Murray, A.2    McElveen, J.E.3    Sahin, U.4    Luxemburger, U.5    Türeci, O.6
  • 27
    • 2642673605 scopus 로고    scopus 로고
    • A survey of the humoral immune response of cancer patients to a panel of human tumor antigens
    • PMID:9547346
    • Stockert E, Jäger E, Chen YT, Scanlan MJ, Gout I, Karbach J, et al. A survey of the humoral immune response of cancer patients to a panel of human tumor antigens. J Exp Med 1998; 187:1349-54; PMID:9547346; http://dx.doi.org/10.1084/jem.187.8.1349
    • (1998) J Exp Med , vol.187 , pp. 1349-1354
    • Stockert, E.1    Jäger, E.2    Chen, Y.T.3    Scanlan, M.J.4    Gout, I.5    Karbach, J.6
  • 28
    • 0033025229 scopus 로고    scopus 로고
    • Antibody immunity to the HER-2/neu oncogenic protein in patients with colorectal cancer
    • PMID:10408800
    • Ward RL, Hawkins NJ, Coomber D, Disis ML. Antibody immunity to the HER-2/neu oncogenic protein in patients with colorectal cancer. Hum Immunol 1999; 60:510-5; PMID:10408800; http://dx.doi. org/10.1016/S0198-8859(99)00003-8
    • (1999) Hum Immunol , vol.60 , pp. 510-515
    • Ward, R.L.1    Hawkins, N.J.2    Coomber, D.3    Disis, M.L.4
  • 29
    • 12544259114 scopus 로고    scopus 로고
    • Endogenous anti-HER2 antibodies block HER2 phosphorylation and signaling through extracellular signal-regulated kinase
    • PMID:15695410
    • Montgomery RB, Makary E, Schiffman K, Goodell V, Disis ML. Endogenous anti-HER2 antibodies block HER2 phosphorylation and signaling through extracellular signal-regulated kinase. Cancer Res 2005; 65:650-6; PMID:15695410
    • (2005) Cancer Res , vol.65 , pp. 650-656
    • Montgomery, R.B.1    Makary, E.2    Schiffman, K.3    Goodell, V.4    Disis, M.L.5
  • 30
    • 20844432364 scopus 로고    scopus 로고
    • NY-ESO-1 is highly expressed in poorprognosis multiple myeloma and induces spontaneous humoral and cellular immune responses
    • PMID:15671442
    • van Rhee F, Szmania SM, Zhan F, Gupta SK, Pomtree M, Lin P, et al. NY-ESO-1 is highly expressed in poorprognosis multiple myeloma and induces spontaneous humoral and cellular immune responses. Blood 2005; 105:3939-44; PMID:15671442; http://dx.doi. org/10.1182/blood-2004-09-3707
    • (2005) Blood , vol.105 , pp. 3939-3944
    • van Rhee, F.1    Szmania, S.M.2    Zhan, F.3    Gupta, S.K.4    Pomtree, M.5    Lin, P.6
  • 31
    • 19944434053 scopus 로고    scopus 로고
    • Dominant B cell epitope from NY-ESO-1 recognized by sera from a wide spectrum of cancer patients: implications as a potential biomarker
    • PMID:15540228
    • Zeng G, Aldridge ME, Wang Y, Pantuck AJ, Wang AY, Liu YX, et al. Dominant B cell epitope from NY-ESO-1 recognized by sera from a wide spectrum of cancer patients: implications as a potential biomarker. Int J Cancer 2005; 114:268-73; PMID:15540228; http://dx.doi.org/10.1002/ijc.20716
    • (2005) Int J Cancer , vol.114 , pp. 268-273
    • Zeng, G.1    Aldridge, M.E.2    Wang, Y.3    Pantuck, A.J.4    Wang, A.Y.5    Liu, Y.X.6
  • 32
    • 3042767922 scopus 로고    scopus 로고
    • NY-ESO-1 expression and its serum immunoreactivity in esophageal cancer
    • PMID:15118836
    • Akcakanat A, Kanda T, Koyama Y, Watanabe M, Kimura E, Yoshida Y, et al. NY-ESO-1 expression and its serum immunoreactivity in esophageal cancer. Cancer Chemother Pharmacol 2004; 54:95-100; PMID:15118836; http://dx.doi.org/10.1007/s00280-004-0768-3
    • (2004) Cancer Chemother Pharmacol , vol.54 , pp. 95-100
    • Akcakanat, A.1    Kanda, T.2    Koyama, Y.3    Watanabe, M.4    Kimura, E.5    Yoshida, Y.6
  • 33
    • 27944486675 scopus 로고    scopus 로고
    • Heterogeneous expression of GAGE, NY-ESO-1, MAGE-A and SSX proteins in esophageal cancer: Implications for immunotherapy
    • PMID:16003736
    • Akcakanat A, Kanda T, Tanabe T, Komukai S, Yajima K, Nakagawa S, et al. Heterogeneous expression of GAGE, NY-ESO-1, MAGE-A and SSX proteins in esophageal cancer: Implications for immunotherapy. Int J Cancer 2006; 118:123-8; PMID:16003736; http://dx.doi.org/10.1002/ijc.21219
    • (2006) Int J Cancer , vol.118 , pp. 123-128
    • Akcakanat, A.1    Kanda, T.2    Tanabe, T.3    Komukai, S.4    Yajima, K.5    Nakagawa, S.6
  • 34
    • 33646098665 scopus 로고    scopus 로고
    • Humoral immune responses of lung cancer patients against tumor antigen NY-ESO-1
    • PMID:15992994
    • Türeci O, Mack U, Luxemburger U, Heinen H, Krummenauer F, Sester M, et al. Humoral immune responses of lung cancer patients against tumor antigen NY-ESO-1. Cancer Lett 2006; 236:64-71; PMID:15992994; http://dx.doi.org/10.1016/j.canlet. 2005.05.008
    • (2006) Cancer Lett , vol.236 , pp. 64-71
    • Türeci, O.1    Mack, U.2    Luxemburger, U.3    Heinen, H.4    Krummenauer, F.5    Sester, M.6
  • 35
    • 3042730062 scopus 로고    scopus 로고
    • Spontaneous tumorspecific humoral and cellular immune responses to NY-ESO-1 in hepatocellular carcinoma
    • PMID:15240519
    • Korangy F, Ormandy LA, Bleck JS, Klempnauer J, Wilkens L, Manns MP, et al. Spontaneous tumorspecific humoral and cellular immune responses to NY-ESO-1 in hepatocellular carcinoma. Clin Cancer Res 2004; 10:4332-41; PMID:15240519; http://dx.doi.org/10.1158/1078-0432.CCR-04-0181
    • (2004) Clin Cancer Res , vol.10 , pp. 4332-4341
    • Korangy, F.1    Ormandy, L.A.2    Bleck, J.S.3    Klempnauer, J.4    Wilkens, L.5    Manns, M.P.6
  • 36
    • 33745839341 scopus 로고    scopus 로고
    • Expression and immunogenicity of NY-ESO-1 in hepatocellular carcinoma
    • PMID:16872310
    • Nakamura S, Nouso K, Noguchi Y, Higashi T, Ono T, Jungbluth A, et al. Expression and immunogenicity of NY-ESO-1 in hepatocellular carcinoma. J Gastroenterol Hepatol 2006; 21:1281-5; PMID:16872310; http://dx.doi.org/10.1111/j.1440-1746.2006.04271.x
    • (2006) J Gastroenterol Hepatol , vol.21 , pp. 1281-1285
    • Nakamura, S.1    Nouso, K.2    Noguchi, Y.3    Higashi, T.4    Ono, T.5    Jungbluth, A.6
  • 37
    • 2442666480 scopus 로고    scopus 로고
    • NY-ESO-1 protein expression and humoral immune responses in prostate cancer
    • PMID:15065093
    • Fosså A, Berner A, Fosså SD, Hernes E, Gaudernack G, Smeland EB. NY-ESO-1 protein expression and humoral immune responses in prostate cancer. Prostate 2004; 59:440-7; PMID:15065093; http://dx.doi. org/10.1002/pros.20025
    • (2004) Prostate , vol.59 , pp. 440-447
    • Fosså, A.1    Berner, A.2    Fosså, S.D.3    Hernes, E.4    Gaudernack, G.5    Smeland, E.B.6
  • 38
    • 0141507936 scopus 로고    scopus 로고
    • NY-ESO-1 and LAGE-1 cancertestis antigens are potential targets for immunotherapy in epithelial ovarian cancer
    • PMID:14522938
    • Odunsi K, Jungbluth AA, Stockert E, Qian F, Gnjatic S, Tammela J, et al. NY-ESO-1 and LAGE-1 cancertestis antigens are potential targets for immunotherapy in epithelial ovarian cancer. Cancer Res 2003; 63:6076-83; PMID:14522938
    • (2003) Cancer Res , vol.63 , pp. 6076-6083
    • Odunsi, K.1    Jungbluth, A.A.2    Stockert, E.3    Qian, F.4    Gnjatic, S.5    Tammela, J.6
  • 40
    • 0030745147 scopus 로고    scopus 로고
    • Perspectives on the significance of altered glycosylation of glycoproteins in cancer
    • PMID:9298689
    • Kim YJ, Varki A. Perspectives on the significance of altered glycosylation of glycoproteins in cancer. Glycoconj J 1997; 14:569-76; PMID:9298689; http://dx.doi.org/10.1023/A:1018580324971
    • (1997) Glycoconj J , vol.14 , pp. 569-576
    • Kim, Y.J.1    Varki, A.2
  • 41
    • 67649847234 scopus 로고    scopus 로고
    • Glycosylation Changes in Cancer
    • In: Varki A, Cummings RD, Esko JD, Freeze HH, Stanley P, Betozzi CR, et al., 2nd ed. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Varki A, Kannagi R, Toole BP. Glycosylation Changes in Cancer. In: Varki A, Cummings RD, Esko JD, Freeze HH, Stanley P, Betozzi CR, et al. Essentials of Glycobiology. 2nd ed. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, 2009:617-32.
    • (2009) Essentials of Glycobiology. , pp. 617-632
    • Varki, A.1    Kannagi, R.2    Toole, B.P.3
  • 42
    • 0020601369 scopus 로고
    • Studies on the effect of inflammation on rat liver and serum sialyltransferase. Evidence that inflammation causes release of Gal beta 1 leads to 4GlcNAc alpha 2 leads to 6 sialyltransferase from liver.
    • PMID:6413502
    • Kaplan HA, Woloski BM, Hellman M, Jamieson JC. Studies on the effect of inflammation on rat liver and serum sialyltransferase. Evidence that inflammation causes release of Gal beta 1 leads to 4GlcNAc alpha 2 leads to 6 sialyltransferase from liver. J Biol Chem 1983; 258:11505-9; PMID:6413502
    • (1983) J Biol Chem , vol.258 , pp. 11505-9
    • Kaplan, H.A.1    Woloski, B.M.2    Hellman, M.3    Jamieson, J.C.4
  • 43
    • 84872754818 scopus 로고    scopus 로고
    • Analysis and functional consequences of increased Fab-sialylation of intravenous immunoglobulin (IVIG) after lectin fractionation
    • PMID:22675478
    • Käsermann F, Boerema DJ, Rüegsegger M, Hofmann A, Wymann S, Zuercher AW, et al. Analysis and functional consequences of increased Fab-sialylation of intravenous immunoglobulin (IVIG) after lectin fractionation. PLoS One 2012; 7:e37243; PMID:22675478; http://dx.doi.org/10.1371/journal.pone.0037243
    • (2012) PLoS One , vol.7
    • Käsermann, F.1    Boerema, D.J.2    Rüegsegger, M.3    Hofmann, A.4    Wymann, S.5    Zuercher, A.W.6
  • 44
    • 0033289903 scopus 로고    scopus 로고
    • Lectin analysis of human immunoglobulin G N-glycan sialylation
    • PMID:11133020
    • Dalziel M, McFarlane I, Axford JS. Lectin analysis of human immunoglobulin G N-glycan sialylation. Glycoconj J 1999; 16:801-7; PMID:11133020; http://dx.doi.org/10.1023/A:1007183915921
    • (1999) Glycoconj J , vol.16 , pp. 801-807
    • Dalziel, M.1    McFarlane, I.2    Axford, J.S.3
  • 45
    • 77956187222 scopus 로고    scopus 로고
    • Analytical and Functional Aspects of Antibody Sialylation
    • In press; PMID:20390325
    • Stadlmann J, Pabst M, Altmann F. Analytical and Functional Aspects of Antibody Sialylation. J Clin Immunol 2010; In press; PMID:20390325; http://dx.doi.org/10.1007/s10875-010-9409-2
    • (2010) J Clin Immunol
    • Stadlmann, J.1    Pabst, M.2    Altmann, F.3
  • 46
    • 79959555556 scopus 로고    scopus 로고
    • Enrichment of sialylated IgG by lectin fractionation does not enhance the efficacy of immunoglobulin G in a murine model of immune thrombocytopenia
    • PMID:21731683
    • Guhr T, Bloem J, Derksen NI, Wuhrer M, Koenderman AH, Aalberse RC, et al. Enrichment of sialylated IgG by lectin fractionation does not enhance the efficacy of immunoglobulin G in a murine model of immune thrombocytopenia. PLoS One 2011; 6:e21246; PMID:21731683; http://dx.doi.org/10.1371/journal. pone.0021246
    • (2011) PLoS One , vol.6
    • Guhr, T.1    Bloem, J.2    Derksen, N.I.3    Wuhrer, M.4    Koenderman, A.H.5    Aalberse, R.C.6
  • 47
    • 34748865088 scopus 로고    scopus 로고
    • Antibody therapeutics: isotype and glycoform selection
    • PMID:17727329
    • Jefferis R. Antibody therapeutics: isotype and glycoform selection. Expert Opin Biol Ther 2007; 7:1401-13; PMID:17727329; http://dx.doi. org/10.1517/14712598.7.9.1401
    • (2007) Expert Opin Biol Ther , vol.7 , pp. 1401-1413
    • Jefferis, R.1
  • 48
    • 33646093725 scopus 로고    scopus 로고
    • Differential glycosylation of polyclonal IgG, IgG-Fc and IgG-Fab isolated from the sera of patients with ANCA-associated systemic vasculitis
    • PMID:16413679
    • Holland M, Yagi H, Takahashi N, Kato K, Savage CO, Goodall DM, et al. Differential glycosylation of polyclonal IgG, IgG-Fc and IgG-Fab isolated from the sera of patients with ANCA-associated systemic vasculitis. Biochim Biophys Acta 2006; 1760:669-77; PMID:16413679; http://dx.doi.org/10.1016/j.bbagen. 2005.11.021
    • (2006) Biochim Biophys Acta , vol.1760 , pp. 669-677
    • Holland, M.1    Yagi, H.2    Takahashi, N.3    Kato, K.4    Savage, C.O.5    Goodall, D.M.6
  • 49
    • 0032462161 scopus 로고    scopus 로고
    • Changes in the galactose content of IgG during humoral immune responses
    • PMID:9754811
    • Lastra GC, Thompson SJ, Lemonidis AS, Elson CJ. Changes in the galactose content of IgG during humoral immune responses. Autoimmunity 1998; 28:25-30; PMID:9754811; http://dx.doi. org/10.3109/08916939808993842
    • (1998) Autoimmunity , vol.28 , pp. 25-30
    • Lastra, G.C.1    Thompson, S.J.2    Lemonidis, A.S.3    Elson, C.J.4
  • 50
    • 77952487132 scopus 로고    scopus 로고
    • Immunoglobulin G galactosylation and sialylation are associated with pregnancy- induced improvement of rheumatoid arthritis and the postpartum flare: results from a large prospective cohort study
    • PMID:20015375
    • van de Geijn FE, Wuhrer M, Selman MH, Willemsen SP, de Man YA, Deelder AM, et al. Immunoglobulin G galactosylation and sialylation are associated with pregnancy- induced improvement of rheumatoid arthritis and the postpartum flare: results from a large prospective cohort study. Arthritis Res Ther 2009; 11:R193; PMID:20015375; http://dx.doi.org/10.1186/ar2892
    • (2009) Arthritis Res Ther , vol.11
    • van de Geijn, F.E.1    Wuhrer, M.2    Selman, M.H.3    Willemsen, S.P.4    de Man, Y.A.5    Deelder, A.M.6
  • 51
    • 79959817309 scopus 로고    scopus 로고
    • Sialylation levels of anti-proteinase 3 antibodies are associated with the activity of granulomatosis with polyangiitis (Wegener's)
    • PMID:21437874
    • Espy C, Morelle W, Kavian N, Grange P, Goulvestre C, Viallon V, et al. Sialylation levels of anti-proteinase 3 antibodies are associated with the activity of granulomatosis with polyangiitis (Wegener's). Arthritis Rheum 2011; 63:2105-15; PMID:21437874; http://dx.doi. org/10.1002/art.30362
    • (2011) Arthritis Rheum , vol.63 , pp. 2105-2115
    • Espy, C.1    Morelle, W.2    Kavian, N.3    Grange, P.4    Goulvestre, C.5    Viallon, V.6
  • 52
    • 77952911607 scopus 로고    scopus 로고
    • Glycan profiling of anti-citrullinated protein antibodies isolated from human serum and synovial fluid
    • PMID:20178128
    • Scherer HU, van der Woude D, Ioan-Facsinay A, el Bannoudi H, Trouw LA, Wang J, et al. Glycan profiling of anti-citrullinated protein antibodies isolated from human serum and synovial fluid. Arthritis Rheum 2010; 62:1620-9; PMID:20178128; http://dx.doi. org/10.1002/art.27414
    • (2010) Arthritis Rheum , vol.62 , pp. 1620-1629
    • Scherer, H.U.1    van der Woude, D.2    Ioan-Facsinay, A.3    el Bannoudi, H.4    Trouw, L.A.5    Wang, J.6
  • 53
    • 36248972262 scopus 로고    scopus 로고
    • Ovarian cancer is associated with changes in glycosylation in both acute-phase proteins and IgG
    • PMID:17884841
    • Saldova R, Royle L, Radcliffe CM, Abd Hamid UM, Evans R, Arnold JN, et al. Ovarian cancer is associated with changes in glycosylation in both acute-phase proteins and IgG. Glycobiology 2007; 17:1344-56; PMID:17884841; http://dx.doi.org/10.1093/glycob/cwm100
    • (2007) Glycobiology , vol.17 , pp. 1344-1356
    • Saldova, R.1    Royle, L.2    Radcliffe, C.M.3    Abd Hamid, U.M.4    Evans, R.5    Arnold, J.N.6
  • 54
    • 61849098877 scopus 로고    scopus 로고
    • Regulated glycosylation patterns of IgG during alloimmune responses against human platelet antigens
    • PMID:18942870
    • Wuhrer M, Porcelijn L, Kapur R, Koeleman CA, Deelder A, de Haas M, et al. Regulated glycosylation patterns of IgG during alloimmune responses against human platelet antigens. J Proteome Res 2009; 8:450-6; PMID:18942870; http://dx.doi.org/10.1021/pr800651j
    • (2009) J Proteome Res , vol.8 , pp. 450-456
    • Wuhrer, M.1    Porcelijn, L.2    Kapur, R.3    Koeleman, C.A.4    Deelder, A.5    de Haas, M.6
  • 55
    • 75749133580 scopus 로고    scopus 로고
    • The pro and anti-inflammatory activities of immunoglobulin G
    • PMID:19995755
    • Lux A, Aschermann S, Biburger M, Nimmerjahn F. The pro and anti-inflammatory activities of immunoglobulin G. Ann Rheum Dis 2010; 69(Suppl 1):i92-6; PMID:19995755; http://dx.doi.org/10.1136/ard.2009.117101
    • (2010) Ann Rheum Dis , vol.69 , Issue.SUPPL 1
    • Lux, A.1    Aschermann, S.2    Biburger, M.3    Nimmerjahn, F.4
  • 56
    • 80055093311 scopus 로고    scopus 로고
    • Update on intravenous immunoglobulins (IVIg) mechanisms of action and off-label use in autoimmune diseases
    • PMID:21864262
    • Katz U, Shoenfeld Y, Zandman-Goddard G. Update on intravenous immunoglobulins (IVIg) mechanisms of action and off-label use in autoimmune diseases. Curr Pharm Des 2011; 17:3166-75; PMID:21864262; http://dx.doi.org/10.2174/138161211798157540
    • (2011) Curr Pharm Des , vol.17 , pp. 3166-3175
    • Katz, U.1    Shoenfeld, Y.2    Zandman-Goddard, G.3
  • 57
    • 33847012894 scopus 로고    scopus 로고
    • Safety of intravenous immunoglobulin (IVIG) therapy
    • PMID:17317619
    • Katz U, Achiron A, Sherer Y, Shoenfeld Y. Safety of intravenous immunoglobulin (IVIG) therapy. Autoimmun Rev 2007; 6:257-9; PMID:17317619; http://dx.doi.org/10.1016/j.autrev.2006.08.011
    • (2007) Autoimmun Rev , vol.6 , pp. 257-259
    • Katz, U.1    Achiron, A.2    Sherer, Y.3    Shoenfeld, Y.4
  • 58
    • 20344364188 scopus 로고    scopus 로고
    • Current approaches to treatment of antibody-mediated rejection
    • PMID:15910400
    • Jordan SC, Vo AA, Tyan D, Nast CC, Toyoda M. Current approaches to treatment of antibody-mediated rejection. Pediatr Transplant 2005; 9:408-15; PMID:15910400; http://dx.doi.org/10.1111/j.1399-3046.2005.00363.x
    • (2005) Pediatr Transplant , vol.9 , pp. 408-415
    • Jordan, S.C.1    Vo, A.A.2    Tyan, D.3    Nast, C.C.4    Toyoda, M.5
  • 59
    • 16444372792 scopus 로고    scopus 로고
    • Post-transplant therapy with high-dose intravenous gammaglobulin: Applications to treatment of antibodymediated rejection
    • PMID:15787786
    • Jordan SC, Vo AA, Toyoda M, Tyan D, Nast CC. Post-transplant therapy with high-dose intravenous gammaglobulin: Applications to treatment of antibodymediated rejection. Pediatr Transplant 2005; 9:155-61; PMID:15787786; http://dx.doi.org/10.1111/j.1399-3046.2005.00256.x
    • (2005) Pediatr Transplant , vol.9 , pp. 155-161
    • Jordan, S.C.1    Vo, A.A.2    Toyoda, M.3    Tyan, D.4    Nast, C.C.5
  • 60
    • 67651027514 scopus 로고    scopus 로고
    • Intravenous immunoglobulin a natural regulator of immunity and inflammation
    • PMID:19584672
    • Jordan SC, Toyoda M, Vo AA. Intravenous immunoglobulin a natural regulator of immunity and inflammation. Transplantation 2009; 88:1-6; PMID:19584672; http://dx.doi.org/10.1097/TP.0b013e3181a9e89a
    • (2009) Transplantation , vol.88 , pp. 1-6
    • Jordan, S.C.1    Toyoda, M.2    Vo, A.A.3
  • 61
    • 33746888249 scopus 로고    scopus 로고
    • Antiinflammatory activity of immunoglobulin G resulting from Fc sialylation
    • PMID:16888140
    • Kaneko Y, Nimmerjahn F, Ravetch JV. Antiinflammatory activity of immunoglobulin G resulting from Fc sialylation. Science 2006; 313:670-3; PMID:16888140; http://dx.doi.org/10.1126/science. 1129594
    • (2006) Science , vol.313 , pp. 670-673
    • Kaneko, Y.1    Nimmerjahn, F.2    Ravetch, J.V.3
  • 62
    • 42349085035 scopus 로고    scopus 로고
    • Recapitulation of IVIG anti-inflammatory activity with a recombinant IgG Fc
    • PMID:18420934
    • Anthony RM, Nimmerjahn F, Ashline DJ, Reinhold VN, Paulson JC, Ravetch JV. Recapitulation of IVIG anti-inflammatory activity with a recombinant IgG Fc. Science 2008; 320:373-6; PMID:18420934; http://dx.doi.org/10.1126/science.1154315
    • (2008) Science , vol.320 , pp. 373-376
    • Anthony, R.M.1    Nimmerjahn, F.2    Ashline, D.J.3    Reinhold, V.N.4    Paulson, J.C.5    Ravetch, J.V.6
  • 63
    • 2442595069 scopus 로고    scopus 로고
    • DC-SIGN binds to HIV-1 glycoprotein 120 in a distinct but overlapping fashion compared with ICAM-2 and ICAM-3
    • PMID:14970226
    • Su SV, Hong P, Baik S, Negrete OA, Gurney KB, Lee B. DC-SIGN binds to HIV-1 glycoprotein 120 in a distinct but overlapping fashion compared with ICAM-2 and ICAM-3. J Biol Chem 2004; 279:19122-32; PMID:14970226; http://dx.doi.org/10.1074/jbc. M400184200
    • (2004) J Biol Chem , vol.279 , pp. 19122-32
    • Su, S.V.1    Hong, P.2    Baik, S.3    Negrete, O.A.4    Gurney, K.B.5    Lee, B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.